Immunological relationships between the diacylglycerol-transporting lipoproteins in the haemolymph of Locusta

Insect flight muscle metabolism

“…Since total protein concentration in the haemolymph remains unaffected during flight or after AKH injection, the changes in the lipoprotein fractions apparently originate from reorganizations of proteins already present in the haemolymph in the resting stage. Immunological evidence pointed to an involvement of the apoprotein from myello w and protein fraction C in the formation of flight-specific lipoproteins ( Van der Horst et al, 1981a), as also suggested by Goldsworthy (1977, 1981). Experiments in which isolated and radiolabelled lipoprotein and protein fractions were reinjected into locusts and dynamics followed have convincingly demonstrated this protein rearrangement Wheeler and Goldsworthy, 1983a, b).…”

Apolipophorin III: a lipid-triggered molecular switch

“…A keyplayer in this transport system is a small protein abundantly found in the hemolymph: apolipophorin III (apoLp-III). Its role in lipid transport was discovered in the late 1970s and early 1980s by research groups at the Utrecht University, Netherlands (Van der Horst et al, 1979, 1981, the University of Hull in England (Wheeler and Goldsworthy, 1983) and at the University of Arizona, USA (Shapiro and Law, 1983;Kawooya et al, 1984Kawooya et al, , 1986. The studies in Utrecht and Hull were performed with the hemimetabolous migratory locust, Locusta migratoria, capable of long-distance flight and notorious as a pest.…”

Chemical and immunological properties of lipophorins from seven insect orders

“…During the process of lipid loading and apoLp-III association the lipophorin particle increases in size [4] and decreases in density [n. Van der Horst et a1 [8] have shown that the unloaded and loaded lipophorins of adult locusts are immunologically related. Upon separation of the apoproteins of Manducu sextu larval lipophorin, Shapiro et a1 [9] showed that apoLp-I and apoLp-I1 are immunologically distinct.…”